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S Bone

Publications and source records attributed to S Bone.

At least 19 recordsLinked to original sources
PubMed1996

Dielectric studies of intermolecular interactions in native DNA.

The concentration dependence of the high frequency dielectric dispersion exhibited by solutions of DNA and the sensitivity of this to the ionic strength of the solution are described. Dielectric data obtained are consistent with a model involving the fluctuation of counterions along short segments of the DNA chain. The concentration and ion strength dependencies are discussed in terms of intermolecular interactions which are considered responsible for the existence of structure in DNA solutions.

Animals↗
PubMed1996

Time-domain reflectometry studies on Halobacterium halobium and Halobacterium marismortui.

The dielectric properties of Halobacterium halobium and Halobacterium marismortui measured over the frequency range 1 MHz to 1 GHz are compared with a single-shell model for interfacial polarization. In the case of Halobacterium halobium, the model shows excellent agreement with the experimental data for reasonable values of membrane and cytoplasmic conductivity and permittivity. For Halobacterium marismortui however, an acceptable fit to the data can only be achieved by invoking a plasma membrane conductivity some three orders of magnitude larger than that of Halobacterium halobium and adding a second high-frequency dielectric dispersion. These observations confirm the findings of a previous study and are consistent with a scheme for Halobacterium marismortui involving thermodynamic compartmentalization of Na and K ions and the existence of a conductive plasma membrane.

Cell Membrane↗
PubMed1996

Dielectric and gravimetric studies of water binding to lysozyme.

Time domain dielectric spectroscopy and hydration isotherm measurements as a function of temperature have been applied to hydrated lysozyme powder. Two dielectric dispersions were identified, the first centred at approximately 8 MHz and a second above 1 GHz. The higher dispersion is considered to be the result of rotational relaxation of water molecules bound to the enzyme. In this case the results indicate the existence of a population of 32 water molecules per lysozyme molecule which are irrotationally bound to the lysozyme structure. A larger population of water molecules is relatively free to respond to the electric field and exhibits a dipole moment close to that of vapour phase water molecules. Multi-temperature hydration isotherm measurements are used to calculate enthalpies and entropies associated with the binding of water to lysozyme. Discontinuities both in dielectric and in thermodynamic characteristics in the range 10-14% hydration are interpreted as a re-ordering of the water structure on the enzyme surface.

Animals↗
PubMed1995

Dielectric studies of ion fluctuation and chain bending in native DNA.

The high-frequency dielectric dispersion exhibited by solutions of native DNA is characterised as a function of electrolyte concentration, counterion type, temperature and pH. The data are interpreted in terms of counterion fluctuation along short segments (subunits) of the DNA chain. From calculation of the subunit length from dielectric relaxation time and increment, information is derived regarding the static and dynamic bending of the DNA chain. Activation enthalpies for the ion fluctuation process are obtained from temperature-dependent dielectric data.

Animals↗
PubMed1993

Time-domain dielectric spectroscopy applied to cell suspensions.

A precision difference time-domain reflectometry (TDR) technique is described for the investigation of the dielectric properties of cell suspensions. The dielectric spectra obtained for erythrocytes using TDR are comparable with those reported in previous dielectric studies employing frequency-domain technique.

Animals↗
PubMed1991

Proton pathways in lysozyme.

Protonic conduction studies are reported for lysozyme as a function of the number of bound water molecules. Lysozyme samples employing proton-injecting palladium black electrodes exhibited conductivities up to eight orders of magnitude greater than those retained between control (copper) electrodes. The results indicate that water involved in multiple hydrogen bond contact with the enzyme together with hydrogen bonded segments of the enzyme structure provide a hydrogen bond network which is capable of supporting considerable protonic conduction.

Copper↗
PubMed1989

Uterine positions and schedules of urination: correlates of differential maternal anogenital stimulation.

Lactating Mongolian gerbils, like lactating Norway rats, reliably lick some pups in their litters more than they lick others. Male gerbil pups are licked more by their dams than are their sisters and some males and some females within each litter are licked more often than are their sibs of the same sex. In the present article, we explore the characteristics of same-sex littermates that are correlated with elicitation of extreme amounts of maternal anogenital licking. We found that both the male pup and the female pup in a litter of gerbils that received the most maternal anogenital licking: (1) released greater quantities of urine and (2) exhibited longer latencies to begin to urinate in response to artificial anogenital stimulation than did the male pup and the female pup in a litter that received the least amount of maternal anogenital licking. We also found that foster mothers rearing Caesarean-delivered litters spent more time licking the anogenital areas of: (1) those male pups that, as fetuses, had occupied uterine locations adjacent to relatively few females and (2) those female pups that, as fetuses, had occupied uterine locations adjacent to relatively many males. We discuss implications of these findings for understanding of how maternal behavior may mediate hormonal effects on the development of young gerbils.

Animals↗
PubMed1988

Time domain reflectrometry: the difference method applied to conductive aqueous solutions.

The precision difference time domain reflectrometry method has been developed for application to conductive aqueous solutions. The sensitivity of the technique has been investigated with protein and polypeptide solutions over the frequency range 100 kHz to 1 GHz. Loss processes with an absorption maximum of 0.3 have been successfully measured and larger dispersions characterised in KCl concentrations as high as 100 mM.

Electric Conductivity↗
PubMed1987

Time-domain reflectrometry studies of water binding and structural flexibility in chymotrypsin.

Time-domain dielectric spectroscopy has been employed to probe the hydration properties and structural flexibility of chymotrypsin (EC 3.4.21.1). The dielectric properties of the hydrated protein above 100 MHz have been used to identify two categories of protein-bound water, the first being irrotationally bound to the protein with a second, relatively weakly bound, having a rotational freedom comparable with that of normal bulk water. A dielectric dispersion observed, centred at 12 MHz, has been attributed to the relaxation of the polar components of the protein structure. This dielectric loss became increasingly significant above a transition in the hydration dependence, where water is relatively weakly bound to the chymotrypsin. This is discussed in terms of the formation of water clusters on the protein surface which screen electrostatic interactions between protein-charged groups.

Chemical Phenomena↗
PubMed1985

Dielectric studies of protein hydration and hydration-induced flexibility.

Dielectric measurements, as a function of hydration, are reported for collagen, cytochrome-c, elastin and lysozyme powders. The hydration dependence of the dispersion that occurs in the frequency range between 10 kHz and 10 GHz has been used to identify two classes of protein-bound water molecules (namely, rotationally hindered or unhindered), as well as the hydration level for the onset of an increasing protein flexibility. Such studies can aid an understanding of the relationship between enzyme activity and structural flexibility, and of hydration-induced changes in the structure and dynamics of protein structures.

Collagen↗
PubMed1978

Electronic properties of some protein--methylglyoxal complexes.

Steady-state conductivity measurements and dielectric measurements in the frequency range 10(-5) to 100 Hz are reported for samples of bovine serum albumin, casein, and lysozyme complexed with methylglyoxal. Compared with the untreated proteins, the brown complexed proteins exhibit an increased conductivity and free electron spin density, together with a low-frequency dielectric dispersion. These results can be taken as evidence that the interaction with methylglyoxal results in the proteins possessing an increased electronic activity associated with the creation of mobile electron holes within the valence band states of the protein molecules.

Aldehydes↗
PubMed1978

Electronic and dielectric properties of protein--methylglyoxal complexes.

Steady-state conduction and dielectric measurements over the frequency range 10(-5) to 10(5) Hz are reported for several proteins that have been complexed with methylglyoxal. Compared with the normal (white) proteins the brown protein--methylglyoxal complexes exhibit a marked increase in electronic conductivity and a pronounced low-frequency dielectric dispersion. The intensity of the brown colour and the electronic activity is directly related to the number of free lysine groups available to react with the methylglyoxal. It is proposed that the methylglyoxal molecules form Schiff bases with the epsilon-amino groups of lysine residues and that these Schiff bases then form a charge-transfer complex with a neighbouring peptide unit. For collagen, in particular, it is found that the electron 'holes' so formed in the polypeptide backbone are capable of long range motion in what can be interpreted as being the valence band of extended electronic states of the protein structure. The protein--methylglyoxal complexes have electronic and dielectric properties similar to those exhibited by the perylene-chloranil charge-transfer complex.

Aldehydes↗